Literature summary for 1.1.1.275 extracted from

Haft, D.H.; Pierce, P.G.; Mayclin, S.J.; Sullivan, A.; Gardberg, A.S.; Abendroth, J.; Begley, D.W.; Phan, I.Q.; Staker, B.L.; Myler, P.J.; Marathias, V.M.; Lorimer, D.D.; Edwards, T.E.
Mycofactocin-associated mycobacterial dehydrogenases with non-exchangeable NAD cofactors (2017), Sci. Rep., 7, 41074.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
to 1.55 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover	Mycobacterium avium
to 1.85 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover	Mycobacterium avium subsp. paratuberculosis
to 1.95 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover	Mycobacterium avium
to 2.0 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover	Mycobacterium avium
to 2.15 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover	Mycobacterium avium

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium avium	A0A0H2ZTN5	-	-
Mycobacterium avium	A0A0H2ZU39	-	-
Mycobacterium avium	A0A0H2ZV91	-	-
Mycobacterium avium	A0A0H2ZWY3	-	-
Mycobacterium avium	A0A0H2ZYS9	-	-
Mycobacterium avium 104	A0A0H2ZTN5	-	-
Mycobacterium avium 104	A0A0H2ZU39	-	-
Mycobacterium avium 104	A0A0H2ZV91	-	-
Mycobacterium avium 104	A0A0H2ZWY3	-	-
Mycobacterium avium 104	A0A0H2ZYS9	-	-
Mycobacterium avium subsp. paratuberculosis	Q73SC8	-	-
Mycobacterium avium subsp. paratuberculosis ATCC BAA-968	Q73SC8	-	-

Synonyms

Synonyms	Comment	Organism
MAP_4146	-	Mycobacterium avium subsp. paratuberculosis
MAV_0896	-	Mycobacterium avium
MAV_1393	-	Mycobacterium avium
MAV_1810	-	Mycobacterium avium
MAV_2598	-	Mycobacterium avium
MAV_2983	-	Mycobacterium avium

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Release 2023.1 (January 2023)